SitesBLAST
Comparing WP_084276347.1 NCBI__GCF_900176045.1:WP_084276347.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
7kb1C Complex of o-acety-l-homoserine aminocarboxypropyltransferase (mety) from thermotoga maritima and a key reaction intermediate (see paper)
34% identity, 95% coverage: 20:396/396 of query aligns to 24:427/428 of 7kb1C
- binding pyridoxal-5'-phosphate: Y57 (= Y53), R59 (= R55)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: G87 (= G83), Q88 (≠ M84), Y112 (≠ F108), N160 (= N151), D185 (= D176), S206 (= S197), T208 (= T199), K209 (= K200), N369 (= N338), I370 (= I339), R404 (= R373)
7kb1A Complex of o-acety-l-homoserine aminocarboxypropyltransferase (mety) from thermotoga maritima and a key reaction intermediate (see paper)
34% identity, 95% coverage: 20:396/396 of query aligns to 24:427/428 of 7kb1A
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid: Y57 (= Y53), R59 (= R55), G87 (= G83), Q88 (≠ M84), Y112 (≠ F108), N160 (= N151), D185 (= D176), S206 (= S197), T208 (= T199), K209 (= K200), N369 (= N338), I370 (= I339), R404 (= R373)
8wkoA Crystal structure of o-acetylhomoserine sulfhydrylase from lactobacillus plantarum in the closed form
32% identity, 99% coverage: 3:395/396 of query aligns to 8:425/425 of 8wkoA
- binding (2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid: G87 (= G83), S88 (≠ M84), Y112 (≠ F108), E155 (= E147), D184 (= D176), T186 (= T178), S206 (= S197), A207 (≠ T198), T208 (= T199), F209 (≠ V201), G212 (= G204), M217 (≠ L209), V369 (≠ I339), A370 (≠ G340)
- binding proline: H213 (≠ Q205), Q284 (≠ L267), S288 (≠ T271)
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
32% identity, 96% coverage: 13:394/396 of query aligns to 17:394/396 of 4hf8A
- active site: R59 (= R55), Y112 (≠ F108), D184 (= D176), K209 (= K200)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G83), I88 (≠ M84), Y112 (≠ F108), E155 (= E147), N159 (= N151), D184 (= D176), S206 (= S197), K209 (= K200), S338 (≠ N338), R373 (= R373)
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
32% identity, 96% coverage: 13:394/396 of query aligns to 17:394/396 of 6egrA
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
32% identity, 94% coverage: 20:393/396 of query aligns to 25:394/397 of 3vk3A
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
32% identity, 94% coverage: 20:393/396 of query aligns to 21:390/393 of 5x30C
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
32% identity, 94% coverage: 20:393/396 of query aligns to 26:395/398 of 1pg8A
- active site: R61 (= R55), Y114 (≠ F108), D186 (= D176), K211 (= K200)
- binding pyridoxal-5'-phosphate: Y59 (= Y53), R61 (= R55), S88 (= S82), G89 (= G83), M90 (= M84), Y114 (≠ F108), D186 (= D176), S208 (= S197), T210 (= T199), K211 (= K200)
P13254 L-methionine gamma-lyase; MGL; Homocysteine desulfhydrase; L-methioninase; EC 4.4.1.11; EC 4.4.1.2 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 3 papers)
32% identity, 94% coverage: 20:393/396 of query aligns to 26:395/398 of P13254
- YSR 59:61 (≠ YAR 53:55) binding
- R61 (= R55) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 83:84) binding in other chain
- Y114 (≠ F108) binding
- C116 (≠ G110) mutation to H: Drastic decrease of the catalytic efficiency of the elimination reaction with L-methionine, by 6700-fold, and increases that with L-cysteine by 7-fold, mainly due to changes in kcat. Loss of ability to catalyze replacement reaction between L-methionine and 2-mercaptoethanol.; mutation to S: 9% of wild-type elimination activity against L-methionine.; mutation to T: 40% of wild-type elimination activity against L-methionine.
- SAT 208:210 (≠ STT 197:199) binding in other chain
- K211 (= K200) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ R251) mutation K->D,E: Marked decrease in elimination activity against both L-methionine and DL-homocysteine.; mutation to M: 50% reduction in alpha,gamma-elimination activity against DL-homocysteine, while retaining elimination activity against L-methionine and L-cysteine.
- D241 (= D252) mutation D->H,R: 5 to 14-fold reduction in alpha,gamma-elimination activity against L-methionine, while no change in affinity for L-methionine.
- R375 (= R373) binding
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
32% identity, 94% coverage: 20:393/396 of query aligns to 20:389/392 of 5x2xA
- active site: R55 (= R55), Y108 (≠ F108), D180 (= D176), K205 (= K200)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y53), R55 (= R55), G83 (= G83), M84 (= M84), Y108 (≠ F108), N155 (= N151), D180 (= D176), S202 (= S197), T204 (= T199), K205 (= K200), V333 (vs. gap), S334 (≠ N338), R369 (= R373)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
32% identity, 94% coverage: 20:393/396 of query aligns to 20:389/392 of 5x2wA
- active site: R55 (= R55), Y108 (≠ F108), D180 (= D176), K205 (= K200)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y53), R55 (= R55), S82 (= S82), G83 (= G83), M84 (= M84), Y108 (≠ F108), D180 (= D176), S202 (= S197), K205 (= K200), V333 (vs. gap), S334 (≠ N338), R369 (= R373)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
32% identity, 96% coverage: 13:394/396 of query aligns to 17:394/396 of 4omaA
- active site: R59 (= R55), Y112 (≠ F108), D184 (= D176), K209 (= K200)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G83), I88 (≠ M84), Y112 (≠ F108), D184 (= D176), S206 (= S197), T208 (= T199), K209 (= K200), V337 (≠ A337), S338 (≠ N338), R373 (= R373)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
32% identity, 96% coverage: 13:394/396 of query aligns to 17:394/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
32% identity, 96% coverage: 13:394/396 of query aligns to 17:394/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
32% identity, 96% coverage: 13:394/396 of query aligns to 17:394/396 of 3jw9A
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
32% identity, 96% coverage: 13:394/396 of query aligns to 16:393/395 of 5m3zA
- active site: R58 (= R55), Y111 (≠ F108), D183 (= D176), K208 (= K200)
- binding norleucine: Y111 (≠ F108), H113 (≠ G110), K208 (= K200), V336 (≠ A337), S337 (≠ N338)
- binding pyridoxal-5'-phosphate: G86 (= G83), I87 (≠ M84), Y111 (≠ F108), E154 (= E147), D183 (= D176), T185 (= T178), S205 (= S197), T207 (= T199), K208 (= K200)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G83), I87 (≠ M84), Y111 (≠ F108), D183 (= D176), S205 (= S197), T207 (= T199), K208 (= K200), V336 (≠ A337), S337 (≠ N338), R372 (= R373)
2cb1A Crystal structure of o-actetyl homoserine sulfhydrylase from thermus thermophilus hb8,oah2.
34% identity, 94% coverage: 20:392/396 of query aligns to 18:402/404 of 2cb1A
- active site: R52 (= R55), F105 (= F108), D176 (= D176), K202 (= K200)
- binding pyridoxal-5'-phosphate: S79 (= S82), G80 (= G83), Q81 (≠ M84), F105 (= F108), D176 (= D176), T178 (= T178), S199 (= S197), T201 (= T199), K202 (= K200)
Sites not aligning to the query:
8erjB Crystal structure of fub7 in complex with e-2-aminocrotonate (see paper)
31% identity, 99% coverage: 4:394/396 of query aligns to 2:425/428 of 8erjB
- binding (2S)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]but-3-enoic acid: G84 (= G83), Q85 (≠ M84), Q88 (≠ I87), Y109 (≠ F108), D181 (= D176), S204 (= S197), K207 (= K200), A368 (= A337), N369 (= N338), T384 (≠ I353), R404 (= R373)
8erjA Crystal structure of fub7 in complex with e-2-aminocrotonate (see paper)
31% identity, 99% coverage: 4:394/396 of query aligns to 2:425/428 of 8erjA
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: S83 (= S82), G84 (= G83), Q85 (≠ M84), Q88 (≠ I87), Y109 (≠ F108), N156 (= N151), D181 (= D176), S204 (= S197), T206 (= T199), K207 (= K200), R404 (= R373)
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
32% identity, 94% coverage: 20:392/396 of query aligns to 24:394/399 of 5dx5A
- active site: R59 (= R55), Y112 (≠ F108), D186 (≠ V175), K211 (= K200)
- binding pyridoxal-5'-phosphate: Y57 (= Y53), R59 (= R55), S86 (= S82), G87 (= G83), M88 (= M84), Y112 (≠ F108), D186 (≠ V175), F189 (≠ T178), S208 (= S197), T210 (= T199), K211 (= K200)
Query Sequence
>WP_084276347.1 NCBI__GCF_900176045.1:WP_084276347.1
MNNFERFQTFVLQQSAAKDGAISPPIIGSAAFSYGDPKSAEAVFAGESRKPLYARMGNPT
NAKLETLLAGIDQGDGAVVTSSGMGAIAAVVSAFLQSGDEIVCVGGLFGGTYAFFTQNLP
RFGIKVRFFKADEEVVLSPQTKMIFCESVGNPSLTVVNFVKLGKLAQKHGILFVVDNTIT
PLLFEPFSWGADIIVYSTTKVISGQSQALGGAIIYKEPRKDLFIHFPFLQNFYENLGKDA
IMGVIKKRALRDFGMSMQAHAAYLTILGLETLPLRIQKATDNAQKLFLALKDKVKVLYAK
NEQYFPFGTGQMMGIDFKSKEDAFTFLEHAKIPFITANIGDSRTLALHMRSTIYRDFKAN
ELEYLGVSEGLVRISVGLENCAMIIEDFENALRKVQ
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory